ID   F4FB98_MICM1            Unreviewed;       372 AA.
AC   F4FB98;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=VAB18032_00795 {ECO:0000313|EMBL:AEB47243.1};
OS   Micromonospora maris (strain DSM 45365 / JCM 31040 / NBRC 109089 / NRRL
OS   B-24793 / AB-18-032) (Verrucosispora maris).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB47243.1, ECO:0000313|Proteomes:UP000008308};
RN   [1] {ECO:0000313|EMBL:AEB47243.1, ECO:0000313|Proteomes:UP000008308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB47243.1,
RC   ECO:0000313|Proteomes:UP000008308};
RX   PubMed=21551311; DOI=10.1128/JB.05041-11;
RA   Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., Bull A.T.,
RA   Kim K.H., Bibb M.J., Choi I.G., Stach J.E.;
RT   "Genome sequence of the abyssomicin- and proximicin-producing marine
RT   actinomycete Verrucosispora maris AB-18-032.";
RL   J. Bacteriol. 193:3391-3392(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP002638; AEB47243.1; -; Genomic_DNA.
DR   RefSeq; WP_013735888.1; NC_015434.1.
DR   AlphaFoldDB; F4FB98; -.
DR   STRING; 263358.VAB18032_00795; -.
DR   KEGG; vma:VAB18032_00795; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008308; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000008308}.
FT   DOMAIN          240..368
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        261
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   372 AA;  39264 MW;  8A761BAFF5140175 CRC64;
     MWQAEVRVDL DAIRENVDRM RAGTSAELMA VVKADGYGHG MVPAARAALD AGATWLGVCT
     LDEALALRAA GIDAPVLAWL LAPGLPLHTG VAADVDLGVA SLPQLDEAVE ASRRAQRPAR
     VHLKIDTGLS RNGATVADWP ALLDAAAKAQ ADGLVEVVGV WSHFVYADMP GHPTTDRQLA
     VFHEGLAMVE RAGLRPRYRH LANSAATLTR PDTHFDLVRP GLAVYGLSPV AGETHGLRPA
     MTARARVMLT KRVPAGTGVS YGHTYTTERD ANLAVVPLGY ADGVPRHASN TGPVQLGGRR
     RTISGRVCMD QFVLDCGDDP VAAGDVATLF GSGADGEPTA DDWAEAVGTI NYEIVTRFGS
     SRVPRVYDGT DS
//